3HAZ
Crystal structure of bifunctional proline utilization A (PutA) protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-05-02 |
Detector | NOIR-1 |
Wavelength(s) | 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 166.763, 195.846, 108.680 |
Unit cell angles | 90.00, 121.48, 90.00 |
Refinement procedure
Resolution | 42.330 - 2.100 |
R-factor | 0.202 |
Rwork | 0.200 |
R-free | 0.23300 |
Structure solution method | combination of Se-Met MAD/SAD and MR |
Starting model (for MR) | Partial model from MAD/SAD phasing from another crystal form |
RMSD bond length | 0.005 |
RMSD bond angle | 0.860 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 43.270 | 43.270 | 2.210 |
High resolution limit [Å] | 2.100 | 6.640 | 2.100 |
Rmerge | 0.103 | 0.070 | 0.412 |
Total number of observations | 20641 | 93890 | |
Number of reflections | 172549 | ||
<I/σ(I)> | 5.386 | 7.2 | 1.8 |
Completeness [%] | 100.0 | 99.6 | 100 |
Redundancy | 3.8 | 3.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 2M Ammonium sulfate, 0.1 M Tris-HCl pH 7.0. N-terminal His tag cleaved by TEV protease, which leaves Gly-His at N-terminus., VAPOR DIFFUSION, SITTING DROP, temperature 298K |